ID   CUE1_ASHGO              Reviewed;         184 AA.
AC   Q756I2;
DT   20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 99.
DE   RecName: Full=Coupling of ubiquitin conjugation to ER degradation protein 1;
GN   Name=CUE1; OrderedLocusNames=AER279W;
OS   Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS   (Yeast) (Eremothecium gossypii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX   NCBI_TaxID=284811;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX   PubMed=15001715; DOI=10.1126/science.1095781;
RA   Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA   Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA   Gaffney T.D., Philippsen P.;
RT   "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT   cerevisiae genome.";
RL   Science 304:304-307(2004).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX   PubMed=23749448; DOI=10.1534/g3.112.002881;
RA   Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT   "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT   loci, numerous translocations, lack of transposons, and distinct gene
RT   duplications.";
RL   G3 (Bethesda) 3:1225-1239(2013).
CC   -!- FUNCTION: Component of the endoplasmic reticulum-associated protein
CC       degradation (ERAD) pathway. Recruits the soluble ubiquitin-conjugating
CC       enzyme UBC7 to the cytoplasmic face of the endoplasmic reticulum
CC       membrane where it functions in degradation of misfolded or regulated
CC       proteins localized in the endoplasmic reticulum (ER) lumen or membrane
CC       via the ubiquitin-proteasome system. Targets the E2 conjugating enzyme
CC       UBC7 to the DOA10 ubiquitin ligase complex, which is part of the ERAD-C
CC       pathway responsible for the rapid degradation of membrane proteins with
CC       misfolded cytoplasmic domains, and to the HRD1 ubiquitin ligase
CC       complex, which is part of the ERAD-L and ERAD-M pathways responsible
CC       for the rapid degradation of soluble lumenal and membrane proteins with
CC       misfolded lumenal domains (ERAD-L), or ER-membrane proteins with
CC       misfolded transmembrane domains (ERAD-M) (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBUNIT: Forms a heterodimer with UBC7. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250};
CC       Single-pass membrane protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the CUE1 family. {ECO:0000305}.
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DR   EMBL; AE016818; AAS52960.1; -; Genomic_DNA.
DR   RefSeq; NP_985136.1; NM_210490.1.
DR   AlphaFoldDB; Q756I2; -.
DR   SMR; Q756I2; -.
DR   STRING; 33169.AAS52960; -.
DR   EnsemblFungi; AAS52960; AAS52960; AGOS_AER279W.
DR   GeneID; 4621347; -.
DR   KEGG; ago:AGOS_AER279W; -.
DR   eggNOG; ENOG502S35Z; Eukaryota.
DR   HOGENOM; CLU_115919_0_0_1; -.
DR   InParanoid; Q756I2; -.
DR   OMA; WLIAPIP; -.
DR   Proteomes; UP000000591; Chromosome V.
DR   GO; GO:1990389; C:CUE1-UBC7 ubiquitin-conjugating enzyme complex; IEA:EnsemblFungi.
DR   GO; GO:0000837; C:Doa10p ubiquitin ligase complex; IEA:EnsemblFungi.
DR   GO; GO:0000839; C:Hrd1p ubiquitin ligase ERAD-L complex; IBA:GO_Central.
DR   GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; IBA:GO_Central.
DR   GO; GO:0016020; C:membrane; IBA:GO_Central.
DR   GO; GO:0043130; F:ubiquitin binding; IBA:GO_Central.
DR   GO; GO:0097027; F:ubiquitin-protein transferase activator activity; IBA:GO_Central.
DR   GO; GO:0097051; P:establishment of protein localization to endoplasmic reticulum membrane; IEA:EnsemblFungi.
DR   GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; IBA:GO_Central.
DR   InterPro; IPR003892; CUE.
DR   InterPro; IPR041158; Cue1_U7BR.
DR   Pfam; PF02845; CUE; 1.
DR   Pfam; PF18499; Cue1_U7BR; 1.
DR   SMART; SM00546; CUE; 1.
DR   PROSITE; PS51140; CUE; 1.
PE   3: Inferred from homology;
KW   Endoplasmic reticulum; Membrane; Reference proteome; Transmembrane;
KW   Transmembrane helix; Ubl conjugation pathway.
FT   CHAIN           1..184
FT                   /note="Coupling of ubiquitin conjugation to ER degradation
FT                   protein 1"
FT                   /id="PRO_0000280669"
FT   TOPO_DOM        1..2
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        3..23
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        24..184
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   DOMAIN          65..107
FT                   /note="CUE"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00468"
FT   REGION          32..63
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          106..145
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        32..50
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        126..145
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   184 AA;  20791 MW;  5BD07F4440694632 CRC64;
     MDQSSALFLA LLLVLFVLVK WFIKTESHPS AQHATVDTGL SSQSTGAAGG RAQGTGAVRR
     RRRPVNDDMI EVVQALAPHL HSEQIRYDLE RSGSVEATVE RYLRGEDFPF PPGYTAPIPP
     ESPQQDSSDP RKRSNIRADD LLQKYDVDPA EDMSAVEFHE LDMDARKRFM VWRARKRMEA
     NLQK